Abstract
Herein, we report an EPR-based method for protease enzymatic characterization and inhibitor screening. This method utilizes dual paramagnetically-labeled probes consisting of a nitroxide spin probe and a Gd3+ion flanking a peptide that could be specifically cleaved by protease caspase-3. Distance-dependent dipolar coupling between the two paramagnetic centers can be modulated by the protease cleavage activity, thus providing a straightforward and convenient method for protease activity detection using EPR spectroscopy under ambient conditions. Moreover, time-course monitoring of the protease-catalyzed cleavage reaction demonstrated that this EPR-based method could not only allow a direct quantitative enzymatic kinetic assessment, but also could be used for protease inhibitor screening, thus holding great potential in drug discovery studies.
Original language | English (US) |
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Pages (from-to) | 9602-9605 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 57 |
Issue number | 75 |
DOIs | |
State | Published - Sep 25 2021 |
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Catalysis
- Ceramics and Composites
- General Chemistry
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry